Linked Life Data

10506206

Source:http://linkedlifedata.com/resource/pubmed/id/10506206

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pubmed-article:10506206pubmed:abstractTextPhosphorylation of the 20-kDa regulatory light chain of myosin catalyzed by a Ca(2+)/calmodulin-dependent myosin light chain kinase is important in the initiation of smooth muscle contraction and other contractile processes in non-muscle cells. It has been previously shown that residues 1-142 of smooth muscle myosin light chain kinase are necessary for high-affinity binding to actin-containing filaments in cells (1). To further localize the region of the kinase required for binding, a series of N-terminal deletion mutants as well as several N-terminal glutathione S-transferase fusion proteins were constructed. Cosedimentation assays showed that a peptide containing residues 1-75 binds to purified smooth muscle myofilaments. Furthermore, the N-terminal peptide was sufficient for high-affinity binding to actin stress fibers in smooth muscle cells in vivo. Alanine scanning mutagenesis in the fusion protein identified residues Asp-30, Phe-31, Arg-32, and Leu-35 as important for binding in vitro. There are two additional DFRXXL motifs located at residues 2-7 and 58-63. The DFR residues in these three motifs were individually replaced by alanine residues in the full-length kinase. Each of these mutations significantly decreased myosin light chain kinase binding to myofilaments in vitro, and each abolished high-affinity binding to actin-containing filaments in smooth muscle cells in vivo. These results identify a unique structural motif comprised of three repeat consensus sequences in the N terminus of myosin light chain kinase necessary for high-affinity binding to actin-containing filaments.lld:pubmed
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pubmed-article:10506206pubmed:articleTitleIdentification of a novel actin binding motif in smooth muscle myosin light chain kinase.lld:pubmed
pubmed-article:10506206pubmed:affiliationDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75235-9040, USA.lld:pubmed
pubmed-article:10506206pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10506206pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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